IGF-1 is a small protein secreted mainly but not solely by the liver and circulating in blood mostly as a complex with various IGF binding proteins in the blood. It has growth-regulating, insulin-like, and mitogenic activities and it is secreted in response to growth hormone stimulation. Recombinant Human IGF-I produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 7655 Dalton.

Source:

E.coli

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Physical Appearance:

White lyophilized (freeze-dried) powder

Formulation:

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Solubility:

It is recommended to reconstitute the lyophilized hIGF-I in sterile 0.4% NaHCO3 adjusted, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

Stability:

Lyophilized hIGF-I although stable at room temperature for several weeks, should be stored desiccated below -18 C. Upon reconstitution at > 0.1 hIGF-I mg/ml and up to 2 2 mg/ml and filter sterilization gsIGF-I can be stored at +4C.

The purified hIGF-I consists of > 97% monomers as determined by gel-filtration chromatography.

Biological Activity:

hIGF-I is fully biologically active when compared to standards. The ED50, calculated by the dose -dependent proliferation of mouse BALBC 3T3 cells is less then 1.0 ng/ml.

Endotoxin:

Endotoxin level as measured by is <0.1EU/ug.

Protein content:

Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.58 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.